Discovery of a twin engine modified from ATP synthase – sciencedaily

For more than 20 years, Makoto Miyata of Osaka University has been studying the sliding motility of parasitic bacteria Mobile mycoplasma (Mr. mobile). It is a mechanism made up of an external “gripping” structure and an internal “motor” – the motor having not yet been clarified at the molecular level. In collaboration with Osaka University and Kanazawa University, his research team used electron microscopy and high-speed atomic force microscopy (high-speed AFM) to reveal that the bacteria’s molecular engine is consisting of two ATP synthase-type complexes, suggesting an unexpected evolution of the protein. Their results were published in mBio.

Based on genetic information, the researchers suggested that the molecular engine of Mr. mobile evolved from a protein that synthesizes ATP, called ATP synthase, although this remains to be confirmed. ATP is an important substance generated in the mitochondria that provides energy that a molecular motor uses for the movement of almost all living things, including Mr. mobile slip.

“It has recently been hypothesized that Mr. mobile, unlike respiratory systems in mitochondria, converts ATP energy into a sliding force with a rotating class of ATP synthase, ”said Makoto Miyata. “To our surprise, we discovered the engine of Mr. mobile to be a chain of two ATP synthase-like molecules, housed in a complex cylindrical structure, ”he continued – something that has never been seen before.

The discovery began when the team extracted a cell from Mr. mobile and by isolating its protein units. Using negative staining electron microscopy, they discovered a dual motor where each motor is structurally similar to ATP synthase. However, the clarification did not end there. “We have to see this ATP synthase dimeric chain in action,” said Noriyuki Kodera of Kanazawa University, “to understand how it facilitates Mr. mobile“Using advanced high-speed AFM technology, developed at the Nano Life Science Institute at Kanazawa University, the team plans to confirm the rotational nature of the molecular motor during ATP hydrolysis. The architecture of the glide engine is like ATP synthase, “it is possible that the strings share a common evolutionary origin,” said Takuma Toyonaga, a researcher at Osaka University.

Toyonaga continued, “This discovery of an ATP synthase created a breakthrough in our understanding of the evolution of cells and proteins and brought us closer to understanding the principles of how motility works, which should serve as the basis for development. of nanoscale devices. and pharmaceuticals. “

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Material provided by Osaka City University. Note: Content can be changed for style and length.

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